1ped: Difference between revisions

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-{{STRUCTURE_1ped|  PDB=1ped  |  SCENE=  }}
-===BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)===
-{{ABSTRACT_PUBMED_15299659}}
-==About this Structure==
+==BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)==
-[[1ped]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PED OCA].
+<StructureSection load='1ped' size='340' side='right'caption='[[1ped]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ped]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PED FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ped FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ped OCA], [https://pdbe.org/1ped PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ped RCSB], [https://www.ebi.ac.uk/pdbsum/1ped PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ped ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ADH_CLOBE ADH_CLOBE] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is active with acetaldehyde and propionaldehyde.<ref>PMID:8349550</ref> <ref>PMID:20102159</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pe/1ped_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ped ConSurf].
+<div style="clear:both"></div>
 ==See Also==
 *[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
-*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]]
+*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
-*[[Chimeras of alcohol dehydrogenases|Chimeras of alcohol dehydrogenases]]
+== References ==
-*[[Tetrameric alcohol dehydrogenases|Tetrameric alcohol dehydrogenases]]
+<references/>
+__TOC__
-==Reference==
+</StructureSection>
-<ref group="xtra">PMID:015299659</ref><references group="xtra"/>
 [[Category: Clostridium beijerinckii]]
-[[Category: Frolow, F.]]
+[[Category: Large Structures]]
-[[Category: Korkhin, Y.]]
+[[Category: Frolow F]]
-[[Category: Nadp]]
+[[Category: Korkhin Y]]
-[[Category: Oxidoreductase]]
-[[Category: Thermostable]]